CYTH1

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CYTH1
Protein PSCD1 PDB 1bc9.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases CYTH1, B2-1, CYTOHESIN-1, D17S811E, PSCD1, SEC7, cytohesin 1
External IDs MGI: 1334257 HomoloGene: 31262 GeneCards: CYTH1
RNA expression pattern
PBB GE PSCD1 202879 s at fs.png

PBB GE PSCD1 202880 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001292018
NM_001292019
NM_004762
NM_017456

NM_001112699
NM_001112700
NM_011180

RefSeq (protein)

NP_001278947
NP_001278948
NP_004753
NP_059430

NP_001106169.1
NP_035310.2
NP_001106169
NP_001106170
NP_035310

Location (UCSC) Chr 17: 78.67 – 78.78 Mb Chr 11: 118.13 – 118.25 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Cytohesin-1 formerly known as Pleckstrin homology, Sec7 and coiled/coil domains 1 (PSCD1) is a protein that in humans is encoded by the CYTH1 gene.[3][4][5]

Function[edit]

Cytohesin-1 (CYTH1) is a member of the cytohesin family. Members of this family have identical structural organization that consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain. The coiled-coil motif is involved in homodimerization, the Sec7 domain contains guanine-nucleotide exchange protein (GEP) activity, and the PH domain interacts with phospholipids and is responsible for association of CYTHs with membranes. Members of this family appear to mediate the regulation of protein sorting and membrane trafficking. The CYTH1 is highly expressed in natural killer and peripheral T cells, and regulates the adhesiveness of integrins at the plasma membrane of lymphocytes. CYTH1 protein is 83% homologous to CYTH2.[5]

Interactions[edit]

CYTH1 has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Liu L, Pohajdak B (September 1992). "Cloning and sequencing of a human cDNA from cytolytic NK/T cells with homology to yeast SEC7". Biochim. Biophys. Acta. 1132 (1): 75–8. doi:10.1016/0167-4781(92)90055-5. PMID 1511013. 
  4. ^ Dixon B, Mansour M, Pohajdak B (April 1993). "Assignment of human B2-1 gene (D17S811E) to chromosome 17qter by PCR analysis of somatic cell hybrids and fluorescence in situ hybridization". Cytogenet. Cell Genet. 63 (1): 42–4. doi:10.1159/000133498. PMID 8449036. 
  5. ^ a b "Entrez Gene: PSCD1 pleckstrin homology, Sec7 and coiled-coil domains 1(cytohesin 1)". 
  6. ^ Schürmann A, Schmidt M, Asmus M, Bayer S, Fliegert F, Koling S, Massmann S, Schilf C, Subauste MC, Voss M, Jakobs KH, Joost HG (April 1999). "The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange factor cytohesin and inhibits the ARF-dependent activation of phospholipase D". J. Biol. Chem. 274 (14): 9744–51. doi:10.1074/jbc.274.14.9744. PMID 10092663. 
  7. ^ Rietzler M, Bittner M, Kolanus W, Schuster A, Holzmann B (October 1998). "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins". J. Biol. Chem. 273 (42): 27459–66. doi:10.1074/jbc.273.42.27459. PMID 9765275. 
  8. ^ Geiger C, Nagel W, Boehm T, van Kooyk Y, Figdor CG, Kremmer E, Hogg N, Zeitlmann L, Dierks H, Weber KS, Kolanus W (June 2000). "Cytohesin-1 regulates beta-2 integrin-mediated adhesion through both ARF-GEF function and interaction with LFA-1". EMBO J. 19 (11): 2525–36. doi:10.1093/emboj/19.11.2525. PMC 212768Freely accessible. PMID 10835351. 
  9. ^ Vitale N, Pacheco-Rodriguez G, Ferrans VJ, Riemenschneider W, Moss J, Vaughan M (July 2000). "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)". J. Biol. Chem. 275 (28): 21331–9. doi:10.1074/jbc.M909642199. PMID 10748148. 

Further reading[edit]